ArticleThe Journal of biological chemistry2009
Triple N-glycosylation in the long S5-P loop regulates the activation and trafficking of the Kv12.2 potassium channel.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Inhibition of cancerous properties of triple-negative MDA-MB-436 cells by targeting the KJournal of physiology and biochemistry · 2025Article
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- Potassium Channels, Glucose Metabolism and Glycosylation in Cancer Cells.International journal of molecular sciences · 2023Review
- Wheat germ agglutinin-conjugated fluorescent pH sensors for visualizing proton fluxes.The Journal of general physiology · 2020Article
- Time and space-resolved quantification of plasma membrane sialylation for measurements of cell function and neurotoxicity.Archives of toxicology · 2020Article
- The Potassium Channel Odyssey: Mechanisms of Traffic and Membrane Arrangement.International journal of molecular sciences · 2019Review
- A Kinetic Map of the Homomeric Voltage-Gated Potassium Channel (Kv) Family.Frontiers in cellular neuroscience · 2019Article
- The role of protein N-glycosylation in neural transmission.Glycobiology · 2014Review
- Inhibition of cardiac pacemaker channel hHCN2 depends on intercalation of lipopolysaccharide into channel-containing membrane microdomains.The Journal of physiology · 2014Article
- The role of Drosophila cytidine monophosphate-sialic acid synthetase in the nervous system.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- The endo-lysosomal system as an NAADP-sensitive acidic Ca(2+) store: role for the two-pore channels.Cell calcium · 2011Review
- Membrane topology of NAADP-sensitive two-pore channels and their regulation by N-linked glycosylation.The Journal of biological chemistry · 2011Article
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7 authors.
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Abstract
Mammalian voltage-dependent potassium (Kv) channels regulate the excitability of nerve and muscle cells. Kv12.2 features the longest S5-P loop among all known mammalian Kv channels with the most N-linked glycosylation sites (three sites). Despite its unique structural features, Kv12.2 is not well characterized. Because glycosylation plays important roles in the folding, trafficking, and function of various Kv channels, we focused on the N-glycosylation of Kv12.2. We show that Kv12.2 is N-glycosylated in Chinese hamster ovary (CHO) cells and in cultured neurons as well as in the mouse brain. As an effect of N-glycosylation on the function of Kv12.2, we demonstrate that removal of sugar chains causes a depolarizing shift in the steady-state activation without a significant reduction in current amplitude. Unlike the previously reported shift for Shaker-type Kv channels, this shift does not appear to be due to negatively charged sialic acid residues in the sugar chains. We next examined the trafficking in CHO cells to address whether the unglycosylated Kv12.2 channels are utilized in vivo. Although double mutants, retaining only one glycosylation site, are trafficked to the surface of CHO cells irrespective of the position of the glycosylated site, unglycosylated channels are not trafficked to the cell surface. Furthermore, we could not detect unglycosylated channels in the mouse brain. Our data suggest that only glycosylated Kv12.2 channels show proper voltage dependence and are utilized in vivo.
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